Structural Flexibility Enhances the Reactivity of the Bioremediator Glycerophosphodiesterase by Fine-Tuning its Mechanism of Hydrolysis
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Hadler, Kieran S; Mitic, Natasa; Ely, Fernanda; Hanson, Graeme; Gahan, Lawrence; Larrabee, James A; Ollis, David; Schenk, Gerhard
Description
The glycerophosphodiesterase from Enterobacter aerogenes (GpdQ) belongs to the family of binuclear metallohydrolases and has attracted recent attention due to its potential in bioremediation. Formation of a catalytically competent binuclear center is promoted by the substrate (Hadler et al. J. Am. Chem. Soc. 2008, 130, 14129). Using the paramagnetic properties of Mn(II), we estimated the Kd values for the metal ions in the α and β sites to be 29 and 344 μM, respectively, in the absence of a...[Show more]
Collections | ANU Research Publications |
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Date published: | 2009 |
Type: | Journal article |
URI: | http://hdl.handle.net/1885/55454 |
Source: | Journal of the American Chemical Society |
DOI: | 10.1021/ja903534f |
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01_Hadler_Structural_Flexibility_2009.pdf | 1.31 MB | Adobe PDF | Request a copy |
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